ID Q04FH2_OENOB Unreviewed; 388 AA.
AC Q04FH2;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Peptidoglycan interpeptide bridge formation enzyme {ECO:0000313|EMBL:ABJ56800.1};
GN OrderedLocusNames=OEOE_0882 {ECO:0000313|EMBL:ABJ56800.1};
OS Oenococcus oeni (strain ATCC BAA-331 / PSU-1).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Oenococcus.
OX NCBI_TaxID=203123 {ECO:0000313|EMBL:ABJ56800.1, ECO:0000313|Proteomes:UP000000774};
RN [1] {ECO:0000313|EMBL:ABJ56800.1, ECO:0000313|Proteomes:UP000000774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-331 / PSU-1 {ECO:0000313|Proteomes:UP000000774};
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA Kozyavkin S., Weimer B., Mills D.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
CC -!- SIMILARITY: Belongs to the FemABX family.
CC {ECO:0000256|ARBA:ARBA00009943}.
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DR EMBL; CP000411; ABJ56800.1; -; Genomic_DNA.
DR RefSeq; WP_011677569.1; NC_008528.1.
DR AlphaFoldDB; Q04FH2; -.
DR STRING; 203123.OEOE_0882; -.
DR DNASU; 4415173; -.
DR KEGG; ooe:OEOE_0882; -.
DR PATRIC; fig|203123.7.peg.895; -.
DR eggNOG; COG2348; Bacteria.
DR HOGENOM; CLU_048411_1_0_9; -.
DR Proteomes; UP000000774; Chromosome.
DR GO; GO:0016755; F:aminoacyltransferase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.90; -; 1.
DR Gene3D; 3.40.630.30; -; 2.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR003447; FEMABX.
DR PANTHER; PTHR36174:SF2; AMINOACYLTRANSFERASE FEMA; 1.
DR PANTHER; PTHR36174; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR Pfam; PF02388; FemAB; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 2.
DR PROSITE; PS51191; FEMABX; 1.
PE 3: Inferred from homology;
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000000774}.
FT COILED 248..282
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 388 AA; 46206 MW; 62D27C43DBD6C30D CRC64;
MQKKYYEDSH QDSYLLGVKE KDEVLLTALM RKIKNHTGDV YEIMGGPLVD FENENNNQII
AFFLKELHKY LKKQHAYYLR IVPNEKTQRV ENNGKVVNYD LKNYSSLYFA EGFIYRSFEQ
VGYGFATPHY EYQKRIEGLN KKTLFQSYSK KTQYSIKKTY EFGITTRNIS YDELEMFHEN
TTKTAKRLGF YDKELSYYQS VYRTFGDNAK FMIAEINLSD YIGHFQEIIR NLKDKIDQMI
LIDSKREKPT KTRQIKELRS QVEQHEKRIV QAKKLIEQYG KKINLAGALF FIQPQEVSYM
FSYTNAEFKN FYGPYRTQAD MLEFALKEKV PVYNFYGVSG DRSGHDGVYE FKKGFQGYMV
DNMGAFILPI NKFRYQFLQT IKKIIRRR
//
